Abstracts (poster) - Wissenschaft Online
Abstracts (poster) - Wissenschaft Online
Abstracts (poster) - Wissenschaft Online
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Peter Hemmerich, Stefanie Weidtkamp-Peters, Christian Hoischen, Lars Schmiedeberg,<br />
Indri Erliandri, Stephan Diekmann<br />
CENP-I as a new epigentic mark at centromere chromatin<br />
Epigenetic marking of a DNA locus may be realized by posttranslational modifications of<br />
nucleosomal histones or by stable binding of a specific protein at that locus. Centromere<br />
identity is believed to be conveyed by CENP-A, a specialized histone H3 analog that<br />
substitutes canonical H3 within centromeric nucleosomes. CENP-A is constitutively<br />
present at centromeres and required for the association of all other kinetochore proteins.<br />
To test whether these epigenetic properties are unique to CENP-A we have assessed the<br />
exchange rates of inner centromere proteins by quantitative microscopy throughout the<br />
cell cycle in living human cells (1). We demonstrate that, in addition to CENP-A, CENP-I<br />
is also a stable centromere component that does at no time exchange with soluble pools<br />
at centromeres. Loading of CENP-I onto centromeric chromatin occurs co-replicationally,<br />
while CENP-A is loaded in early G1. A subfraction of CENP-H (~20%) also stays stably<br />
bound to centromeres throughout the cell cyle. In contrast, CENP-B, CENP-C, and<br />
hMis12 turn over completely at centromeres with residence times ranging between<br />
seconds to hours. Our data reveal a wide range of cell cycle-specific assembly plasticity<br />
of the centromere during the cell-cycle and identify CENP-I as a potentially additional<br />
epigentic marker at centromeres.<br />
Literature<br />
(1) Hemmerich et al., J. Cell Biol. (2008) in press<br />
contact:<br />
PhD Peter Hemmerich<br />
Leibniz Institute for Age Research<br />
Fritz-Lipmann-Institute<br />
phemmer@fli-leibniz.de<br />
Beutenbergstr. 11<br />
07745 Jena (Germany)